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Article

Effect of L110M Mutation on the Structure and Stability of ATTR(105-115) Peptide Assembly: A Computational Study.

Proteins - 1 Feb 2026

Bhattacharya Prabuddha, Mittal Sumit

Abstract excerpt

The mechanisms driving amyloid assembly have long intrigued structural biologists, as they offer insights into systemic fibrotic changes and the dynamic behavior of transthyretin (TTR) aggregation, crucial for developing amyloid-targeted therapies. In TTR-associated amyloidosis, amyloid fibrils form via destabilization of the tetramer into dimers and monomers. While many TTR mutations have been studied, the...

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Amyloid
Amyloid Neuropathies, Familial
Hydrogen Bonding
Prealbumin
Principal Component Analysis

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Protein Aggregation, Pathological

Protein Conformation, beta-Strand

Protein Stability

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Identifiers

PMID: 40905130
DOI: 10.1002/prot.70046

Genes

TTR

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 1 Sept 2026.

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Effect of L110M Mutation on the Structure and Stability of ATTR(105-115) Peptide Assembly: A Computational Study.PMID 40905130Read ↗

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